Article: Cumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix

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TitleCumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix
AuthorsChung, MK2
Chiu, PCN2
Lee, CL2
Pang, RTK2
Ng, EHY2
Lee, KF2
Koistinen, R1
Koistinen, H1
Seppala, M1
Yeung, WSB2
KeywordsΑ2-Macroglobulin
Cumulus Matrix
Glycodelin
Hyaluronic Acid
Spermatozoa
Issue Date2009
PublisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
CitationHuman Reproduction, 2009, v. 24 n. 11, p. 2856-2867 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep265
AbstractBACKGROUNDGlycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix.METHODSGIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS Mass spectrometry analysis suggested that GIP contained the N-terminal region of α2-macroglobulin, confirmed by western blot with anti-α2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled α2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and-F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.
ISSN0268-1161
2011 Impact Factor: 4.475
2011 SCImago Journal Rankings: 0.345
DOIhttp://dx.doi.org/10.1093/humrep/dep265
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorChung, MK
dc.contributor.authorChiu, PCN
dc.contributor.authorLee, CL
dc.contributor.authorPang, RTK
dc.contributor.authorNg, EHY
dc.contributor.authorLee, KF
dc.contributor.authorKoistinen, R
dc.contributor.authorKoistinen, H
dc.contributor.authorSeppala, M
dc.contributor.authorYeung, WSB
dc.date.accessioned2012-10-30T06:29:33Z
dc.date.available2012-10-30T06:29:33Z
dc.date.issued2009
dc.description.abstractBACKGROUNDGlycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix.METHODSGIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS Mass spectrometry analysis suggested that GIP contained the N-terminal region of α2-macroglobulin, confirmed by western blot with anti-α2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled α2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and-F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationHuman Reproduction, 2009, v. 24 n. 11, p. 2856-2867 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep265
dc.identifier.citeulike5426223
dc.identifier.doihttp://dx.doi.org/10.1093/humrep/dep265
dc.identifier.epage2867
dc.identifier.issn0268-1161
2011 Impact Factor: 4.475
2011 SCImago Journal Rankings: 0.345
dc.identifier.issue11
dc.identifier.scopuseid_2-s2.0-70350510673
dc.identifier.spage2856
dc.identifier.urihttp://hdl.handle.net/10722/173353
dc.identifier.volume24
dc.languageeng
dc.publisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
dc.publisher.placeUnited Kingdom
dc.relation.ispartofHuman Reproduction
dc.relation.referencesReferences in Scopus
dc.subjectΑ2-Macroglobulin
dc.subjectCumulus Matrix
dc.subjectGlycodelin
dc.subjectHyaluronic Acid
dc.subjectSpermatozoa
dc.titleCumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix
dc.typeArticle
Author Affiliations
  1. Helsingin Yliopisto
  2. The University of Hong Kong